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Conserved domains on  [gi|1007389400|ref|NP_001308140|]
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heterogeneous nuclear ribonucleoprotein U-like protein 1 isoform d [Homo sapiens]

Protein Classification

ATP-binding protein( domain architecture ID 11596353)

ATP-binding protein with an AAA (ATPases Associated with various cellular Activities) domain may function as an ATPase; similar to NEDD4-binding protein 2-like 1/2 (N4BP2L1 and N4BP2L2), whose functions are not clear

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SPRY_hnRNP cd12884
SPRY domain in heterogeneous nuclear ribonucleoprotein U-like (hnRNP) protein 1; This domain, ...
 111-288 3.82e-116

SPRY domain in heterogeneous nuclear ribonucleoprotein U-like (hnRNP) protein 1; This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of heterogeneous nuclear ribonucleoprotein U-like (hnRNP) protein 1 (also known as HNRPUL1 ) which is a major constituent of nuclear matrix or scaffold and binds directly to DNA sequences through the N-terminal acidic region named serum amyloid P (SAP). Its function is specifically modulated by E1B-55kDa in adenovirus-infected cells. HNRPUL1 also participates in ATR protein kinase signaling pathways during adenovirus infection. Two transcript variants encoding different isoforms have been found for this gene. When associated with bromodomain-containing protein 7 (BRD7), it activates transcription of glucocorticoid-responsive promoter in the absence of ligand-stimulation.


:

Pssm-ID: 293942  Cd Length: 177  Bit Score: 347.65  E-value: 3.82e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007389400 111 VAIDTYNCDLHFKVARDRSSGYPLTIEGFAYLWSGARASYGVRRGRVCFEMKINEEISVKHLPSTEPDPHVVRIGWSLDS 190
Cdd:cd12884     1 VCLDTYNSDLHLKISKDRYSASPLTDEGFAYLWAGARATYGVTKGKVCFEVKVTENLPVKHLPTEETDPHVVRVGWSVDS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007389400 191 CSTQLGEEPFSYGYGGTGKKSTNSRFENYGDKFAENDVIGCFADFEcGNDVELSFTKNGKWMGIAFRIQKEALGGQALYP 270
Cdd:cd12884    81 SSLQLGEEEFSYGYGSTGKKSTNCKFEDYGEPFGENDVIGCYLDFE-SEPVEISFSKNGKDLGVAFKISKEELGGKALFP 159

                         170
                  ....*....|....*...
gi 1007389400 271 HVLVKNCAVEFNFGQRAE 288
Cdd:cd12884   160 HVLTKNCAVEVNFGQKEE 177
AAA_33 pfam13671
AAA domain; This family of domains contain only a P-loop motif, that is characteriztic of the ...
 324-468 5.34e-32

AAA domain; This family of domains contain only a P-loop motif, that is characteriztic of the AAA superfamily. Many of the proteins in this family are just short fragments so there is no Walker B motif.


:

Pssm-ID: 463952 [Multi-domain]  Cd Length: 143  Bit Score: 121.26  E-value: 5.34e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007389400 324 LMMVGLPAAGKTTWAIKHAASNPskkYNILGTNAIMDKMRVMGLRRQRNYAGRWDVliqqATQCLNRLIQIAARKKRNYI 403
Cdd:pfam13671   2 ILLVGLPGSGKSTLARRLLEELG---AVRLSSDDERKRLFGEGRPSISYYTDATDR----TYERLHELARIALRAGRPVI 74

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1007389400 404 LDQTNVYGSAQRRKMRPFE--GFQRKAIVICPTDEDLKDRTIKRTDEEGK--DVPDHAVLEMKANFTLP 468
Cdd:pfam13671  75 LDATNLRRDERARLLALAReyGVPVRIVVFEAPEEVLRERLAARARAGGDpsDVPEEVLDRQKARFEPP 143
 
Name Accession Description Interval E-value
SPRY_hnRNP cd12884
SPRY domain in heterogeneous nuclear ribonucleoprotein U-like (hnRNP) protein 1; This domain, ...
 111-288 3.82e-116

SPRY domain in heterogeneous nuclear ribonucleoprotein U-like (hnRNP) protein 1; This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of heterogeneous nuclear ribonucleoprotein U-like (hnRNP) protein 1 (also known as HNRPUL1 ) which is a major constituent of nuclear matrix or scaffold and binds directly to DNA sequences through the N-terminal acidic region named serum amyloid P (SAP). Its function is specifically modulated by E1B-55kDa in adenovirus-infected cells. HNRPUL1 also participates in ATR protein kinase signaling pathways during adenovirus infection. Two transcript variants encoding different isoforms have been found for this gene. When associated with bromodomain-containing protein 7 (BRD7), it activates transcription of glucocorticoid-responsive promoter in the absence of ligand-stimulation.


Pssm-ID: 293942  Cd Length: 177  Bit Score: 347.65  E-value: 3.82e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007389400 111 VAIDTYNCDLHFKVARDRSSGYPLTIEGFAYLWSGARASYGVRRGRVCFEMKINEEISVKHLPSTEPDPHVVRIGWSLDS 190
Cdd:cd12884     1 VCLDTYNSDLHLKISKDRYSASPLTDEGFAYLWAGARATYGVTKGKVCFEVKVTENLPVKHLPTEETDPHVVRVGWSVDS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007389400 191 CSTQLGEEPFSYGYGGTGKKSTNSRFENYGDKFAENDVIGCFADFEcGNDVELSFTKNGKWMGIAFRIQKEALGGQALYP 270
Cdd:cd12884    81 SSLQLGEEEFSYGYGSTGKKSTNCKFEDYGEPFGENDVIGCYLDFE-SEPVEISFSKNGKDLGVAFKISKEELGGKALFP 159

                         170
                  ....*....|....*...
gi 1007389400 271 HVLVKNCAVEFNFGQRAE 288
Cdd:cd12884   160 HVLTKNCAVEVNFGQKEE 177
AAA_33 pfam13671
AAA domain; This family of domains contain only a P-loop motif, that is characteriztic of the ...
 324-468 5.34e-32

AAA domain; This family of domains contain only a P-loop motif, that is characteriztic of the AAA superfamily. Many of the proteins in this family are just short fragments so there is no Walker B motif.


Pssm-ID: 463952 [Multi-domain]  Cd Length: 143  Bit Score: 121.26  E-value: 5.34e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007389400 324 LMMVGLPAAGKTTWAIKHAASNPskkYNILGTNAIMDKMRVMGLRRQRNYAGRWDVliqqATQCLNRLIQIAARKKRNYI 403
Cdd:pfam13671   2 ILLVGLPGSGKSTLARRLLEELG---AVRLSSDDERKRLFGEGRPSISYYTDATDR----TYERLHELARIALRAGRPVI 74

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1007389400 404 LDQTNVYGSAQRRKMRPFE--GFQRKAIVICPTDEDLKDRTIKRTDEEGK--DVPDHAVLEMKANFTLP 468
Cdd:pfam13671  75 LDATNLRRDERARLLALAReyGVPVRIVVFEAPEEVLRERLAARARAGGDpsDVPEEVLDRQKARFEPP 143
SPRY pfam00622
SPRY domain; SPRY Domain is named from SPla and the RYanodine Receptor and it is found in many ...
 175-286 3.07e-28

SPRY domain; SPRY Domain is named from SPla and the RYanodine Receptor and it is found in many eukaryotic proteins with a wide range of functions. It is a protein-interaction module involved in many important signalling pathways like RNA processing, regulation of histone H3 methylation, innate immunity or embryonic development. It can be divided into 11 subfamilies based on amino acid sequence similarity or the presence of additional protein domains. The greater SPRY family is divided into the SPRY/B30.2 (which contains a PRY extension at the N-terminal) and SPRY-only sub-families which are preceded by a subdomain that is structurally similar to the PRY region. SPRY/B30.2 structures revealed a bent beta-sandwich fold comprised of two beta-sheets. Distant homologs are domains in butyrophilin/ marenostrin/pyrin.


Pssm-ID: 459877  Cd Length: 121  Bit Score: 109.74  E-value: 3.07e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007389400 175 TEPDPHVVRIGWSLDSCSTQ----LGEEPFSYGYGG-TGKKSTNSRFENYGD-KFAENDVIGCFADFECGndvELSFTKN 248
Cdd:pfam00622   9 FGQDGGGWRVGWATKSVPRKgerfLGDESGSWGYDGwTGKKYWASTSPLTGLpLFEPGDVIGCFLDYEAG---TISFTKN 85

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1007389400 249 GKWMGIAFRIQKealGGQALYPHV-LVKNCAVEFNFGQR 286
Cdd:pfam00622  86 GKSLGYAFRDVP---FAGPLFPAVsLGAGEGLKFNFGLR 121
SPRY smart00449
Domain in SPla and the RYanodine Receptor; Domain of unknown function. Distant homologues are ...
 154-285 3.74e-27

Domain in SPla and the RYanodine Receptor; Domain of unknown function. Distant homologues are domains in butyrophilin/marenostrin/pyrin homologues.


Pssm-ID: 214669  Cd Length: 122  Bit Score: 106.61  E-value: 3.74e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007389400  154 RGRVCFEMKINeeisvkhlpstepDPHVVRIGWSLDSCS----TQLGEEPFSYGYGGT-GKKSTNSRFENYGDKFAE-ND 227
Cdd:smart00449   1 SGRHYFEVEIG-------------DGGHWRVGVATKSVPrgyfALLGEDKGSWGYDGDgGKKYHNSTGPEYGLPLQEpGD 67

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007389400  228 VIGCFADFECGndvELSFTKNGK-WMGIAFRiqkEALGGQALYPHVLVKN-CAVEFNFGQ 285
Cdd:smart00449  68 VIGCFLDLEAG---TISFYKNGKyLHGLAFF---DVKFSGPLYPAFSLGSgNSVRLNFGP 121
COG4639 COG4639
Predicted kinase [General function prediction only];
320-478 9.46e-08

Predicted kinase [General function prediction only];


Pssm-ID: 443677 [Multi-domain]  Cd Length: 145  Bit Score: 51.75  E-value: 9.46e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007389400 320 ECEILMMVGLPAAGKTTWAIKHAASNPskkynILGTnaimDKMRVM-GLRR--QRNYAGRWDVLIQQATQCLnrliqiaa 396
Cdd:COG4639     1 MLSLVVLIGLPGSGKSTFARRLFAPTE-----VVSS----DDIRALlGGDEndQSAWGDVFQLAHEIARARL-------- 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007389400 397 RKKRNYILDQTNVygsaQRRKMRPFEGFQRK------AIVICPTDEDLKDRTIKRTdeegKDVPDHAVLEMKANF-TLPD 469
Cdd:COG4639    64 RAGRLTVVDATNL----QREARRRLLALARAygalvvAVVLDVPLEVCLARNAARD----RQVPEEVIRRMLRRLrRPPL 135


                  ....*....
gi 1007389400 470 VGDFLDEVL 478
Cdd:COG4639   136 PEEGFRVVY 144
pseT PHA02530
polynucleotide kinase; Provisional
 320-352 5.32e-03

polynucleotide kinase; Provisional


Pssm-ID: 222856 [Multi-domain]  Cd Length: 300  Bit Score: 39.62  E-value: 5.32e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1007389400 320 ECEILMMVGLPAAGKTTWAIKHAASNPsKKYNI 352
Cdd:PHA02530    1 MMKIILTVGVPGSGKSTWAREFAAKNP-KAVNV 32
 
Name Accession Description Interval E-value
SPRY_hnRNP cd12884
SPRY domain in heterogeneous nuclear ribonucleoprotein U-like (hnRNP) protein 1; This domain, ...
 111-288 3.82e-116

SPRY domain in heterogeneous nuclear ribonucleoprotein U-like (hnRNP) protein 1; This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of heterogeneous nuclear ribonucleoprotein U-like (hnRNP) protein 1 (also known as HNRPUL1 ) which is a major constituent of nuclear matrix or scaffold and binds directly to DNA sequences through the N-terminal acidic region named serum amyloid P (SAP). Its function is specifically modulated by E1B-55kDa in adenovirus-infected cells. HNRPUL1 also participates in ATR protein kinase signaling pathways during adenovirus infection. Two transcript variants encoding different isoforms have been found for this gene. When associated with bromodomain-containing protein 7 (BRD7), it activates transcription of glucocorticoid-responsive promoter in the absence of ligand-stimulation.


Pssm-ID: 293942  Cd Length: 177  Bit Score: 347.65  E-value: 3.82e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007389400 111 VAIDTYNCDLHFKVARDRSSGYPLTIEGFAYLWSGARASYGVRRGRVCFEMKINEEISVKHLPSTEPDPHVVRIGWSLDS 190
Cdd:cd12884     1 VCLDTYNSDLHLKISKDRYSASPLTDEGFAYLWAGARATYGVTKGKVCFEVKVTENLPVKHLPTEETDPHVVRVGWSVDS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007389400 191 CSTQLGEEPFSYGYGGTGKKSTNSRFENYGDKFAENDVIGCFADFEcGNDVELSFTKNGKWMGIAFRIQKEALGGQALYP 270
Cdd:cd12884    81 SSLQLGEEEFSYGYGSTGKKSTNCKFEDYGEPFGENDVIGCYLDFE-SEPVEISFSKNGKDLGVAFKISKEELGGKALFP 159

                         170
                  ....*....|....*...
gi 1007389400 271 HVLVKNCAVEFNFGQRAE 288
Cdd:cd12884   160 HVLTKNCAVEVNFGQKEE 177
SPRY_DDX1 cd12873
SPRY domain associated with DEAD box gene DDX1; This SPRY domain is associated with the DEAD ...
 127-285 3.18e-42

SPRY domain associated with DEAD box gene DDX1; This SPRY domain is associated with the DEAD box gene, DDX1, an RNA-dependent ATPase involved in HIV-1 Rev function and virus replication. It is suggested that DDX1 acts as a cellular cofactor by promoting oligomerization of Rev on the Rev response element (RRE). DDX1 RNA is overexpressed in breast cancer, data showing a strong and independent association between poor prognosis and deregulation of the DEAD box protein DDX1, thus potentially serving as an effective prognostic biomarker for early recurrence in primary breast cancer. DDX1 also interacts with RelA and enhances nuclear factor kappaB-mediated transcription. DEAD-box proteins are associated with all levels of RNA metabolism and function, and have been implicated in translation initiation, transcription, RNA splicing, ribosome assembly, RNA transport, and RNA decay.


Pssm-ID: 293933  Cd Length: 155  Bit Score: 150.42  E-value: 3.18e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007389400 127 DRSSGYPLTIEG------FAYLWSGARASYGVR-RGRVCFEMKINEEisvkhlpstepdpHVVRIGWSLDSCSTQLGEEP 199
Cdd:cd12873     5 DRDAALAISPDGllcqsrEEKGWQGCRATKGVKgKGKYYYEVTVTDE-------------GLCRVGWSTEDASLDLGTDK 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007389400 200 FSYGYGGTGKKSTNSRFENYGDKFAENDVIGCFADFECGndvELSFTKNGKWMGIAFRIqKEALGGQALYPHVLVKNCAV 279
Cdd:cd12873    72 FGFGYGGTGKKSHGRQFDDYGEPFGLGDVIGCYLDLDNG---TISFSKNGKDLGKAFDI-PPHLRNSALFPAVCLKNAEV 147


                  ....*.
gi 1007389400 280 EFNFGQ 285
Cdd:cd12873   148 EFNFGD 153
AAA_33 pfam13671
AAA domain; This family of domains contain only a P-loop motif, that is characteriztic of the ...
 324-468 5.34e-32

AAA domain; This family of domains contain only a P-loop motif, that is characteriztic of the AAA superfamily. Many of the proteins in this family are just short fragments so there is no Walker B motif.


Pssm-ID: 463952 [Multi-domain]  Cd Length: 143  Bit Score: 121.26  E-value: 5.34e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007389400 324 LMMVGLPAAGKTTWAIKHAASNPskkYNILGTNAIMDKMRVMGLRRQRNYAGRWDVliqqATQCLNRLIQIAARKKRNYI 403
Cdd:pfam13671   2 ILLVGLPGSGKSTLARRLLEELG---AVRLSSDDERKRLFGEGRPSISYYTDATDR----TYERLHELARIALRAGRPVI 74

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1007389400 404 LDQTNVYGSAQRRKMRPFE--GFQRKAIVICPTDEDLKDRTIKRTDEEGK--DVPDHAVLEMKANFTLP 468
Cdd:pfam13671  75 LDATNLRRDERARLLALAReyGVPVRIVVFEAPEEVLRERLAARARAGGDpsDVPEEVLDRQKARFEPP 143
SPRY pfam00622
SPRY domain; SPRY Domain is named from SPla and the RYanodine Receptor and it is found in many ...
 175-286 3.07e-28

SPRY domain; SPRY Domain is named from SPla and the RYanodine Receptor and it is found in many eukaryotic proteins with a wide range of functions. It is a protein-interaction module involved in many important signalling pathways like RNA processing, regulation of histone H3 methylation, innate immunity or embryonic development. It can be divided into 11 subfamilies based on amino acid sequence similarity or the presence of additional protein domains. The greater SPRY family is divided into the SPRY/B30.2 (which contains a PRY extension at the N-terminal) and SPRY-only sub-families which are preceded by a subdomain that is structurally similar to the PRY region. SPRY/B30.2 structures revealed a bent beta-sandwich fold comprised of two beta-sheets. Distant homologs are domains in butyrophilin/ marenostrin/pyrin.


Pssm-ID: 459877  Cd Length: 121  Bit Score: 109.74  E-value: 3.07e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007389400 175 TEPDPHVVRIGWSLDSCSTQ----LGEEPFSYGYGG-TGKKSTNSRFENYGD-KFAENDVIGCFADFECGndvELSFTKN 248
Cdd:pfam00622   9 FGQDGGGWRVGWATKSVPRKgerfLGDESGSWGYDGwTGKKYWASTSPLTGLpLFEPGDVIGCFLDYEAG---TISFTKN 85

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1007389400 249 GKWMGIAFRIQKealGGQALYPHV-LVKNCAVEFNFGQR 286
Cdd:pfam00622  86 GKSLGYAFRDVP---FAGPLFPAVsLGAGEGLKFNFGLR 121
SPRY smart00449
Domain in SPla and the RYanodine Receptor; Domain of unknown function. Distant homologues are ...
 154-285 3.74e-27

Domain in SPla and the RYanodine Receptor; Domain of unknown function. Distant homologues are domains in butyrophilin/marenostrin/pyrin homologues.


Pssm-ID: 214669  Cd Length: 122  Bit Score: 106.61  E-value: 3.74e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007389400  154 RGRVCFEMKINeeisvkhlpstepDPHVVRIGWSLDSCS----TQLGEEPFSYGYGGT-GKKSTNSRFENYGDKFAE-ND 227
Cdd:smart00449   1 SGRHYFEVEIG-------------DGGHWRVGVATKSVPrgyfALLGEDKGSWGYDGDgGKKYHNSTGPEYGLPLQEpGD 67

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007389400  228 VIGCFADFECGndvELSFTKNGK-WMGIAFRiqkEALGGQALYPHVLVKN-CAVEFNFGQ 285
Cdd:smart00449  68 VIGCFLDLEAG---TISFYKNGKyLHGLAFF---DVKFSGPLYPAFSLGSgNSVRLNFGP 121
SPRY_Ash2 cd12872
SPRY domain in Ash2; This SPRY domain is found at the C-terminus of Ash2 (absent, small, or ...
 143-284 3.97e-22

SPRY domain in Ash2; This SPRY domain is found at the C-terminus of Ash2 (absent, small, or homeotic discs 2) -like proteins, core components of all mixed-lineage leukemia (MLL) family histone methyltransferases. Ash2 is a member of the trithorax group of transcriptional regulators of the Hox genes. Recent studies show that the SPRY domain of Ash2 mediates the interaction with RbBP5 and has an important role in regulating the methyltransferase activity of MLL complexes. In yeast, Ash2 is involved in histone methylation and is required for the earliest stages of embryogenesis.


Pssm-ID: 293932  Cd Length: 150  Bit Score: 93.35  E-value: 3.97e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007389400 143 WSGARASYGVRRGRVCFEMKINEeisvkhlPSTEPDPHvVRIGWSLDSCSTQ--LGEEPFSYGYGG-TGKKSTNSRFENY 219
Cdd:cd12872    16 YRMARANHGVREGKWYFEVKILE-------GGGTETGH-VRVGWSRREASLQapVGYDKYSYAIRDkDGSKFHQSRGKPY 87

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1007389400 220 GDK-FAENDVIGCFADFEcgndvELSFTKNGKWMGIAFRIQKEALGgqaLYPHV-LVKNCAVEFNFG 284
Cdd:cd12872    88 GEPgFKEGDVIGFLITLP-----KIEFFKNGKSQGVAFEDIYGTGG---YYPAVsLYKGATVTINFG 146
SPRY cd11709
SPRY domain; SPRY domains, first identified in the SP1A kinase of Dictyostelium and rabbit ...
 155-282 5.01e-21

SPRY domain; SPRY domains, first identified in the SP1A kinase of Dictyostelium and rabbit Ryanodine receptor (hence the name), are homologous to B30.2. SPRY domains have been identified in at least 11 protein families, covering a wide range of functions, including regulation of cytokine signaling (SOCS), RNA metabolism (DDX1 and hnRNP), immunity to retroviruses (TRIM5alpha), intracellular calcium release (ryanodine receptors or RyR) and regulatory and developmental processes (HERC1 and Ash2L). B30.2 also contains residues in the N-terminus that form a distinct PRY domain structure; i.e. B30.2 domain consists of PRY and SPRY subdomains. B30.2 domains comprise the C-terminus of three protein families: BTNs (receptor glycoproteins of immunoglobulin superfamily); several TRIM proteins (composed of RING/B-box/coiled-coil or RBCC core); Stonutoxin (secreted poisonous protein of the stonefish Synanceia horrida). TRIM/RBCC proteins are involved in a variety of processes, including apoptosis, cell cycle regulation, cell growth, senescence, viral response, meiosis, cell differentiation, and vesicular transport. Genes belonging to this family are implicated in several human diseases that vary from cancer to rare genetic syndromes. The PRY-SPRY domain in these TRIM families is suggested to serve as the target binding site. While SPRY domains are evolutionarily ancient, B30.2 domains are a more recent adaptation where the SPRY/PRY combination is a possible component of immune defense. Mutations found in the SPRY-containing proteins have shown to cause Mediterranean fever and Opitz syndrome.


Pssm-ID: 293931  Cd Length: 118  Bit Score: 89.03  E-value: 5.01e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007389400 155 GRVCFEMKINEEISvkhlpstepdpHVVRIGWSLDSCSTQ----LGEEPFSYGYGGTGKKS-TNSRFENYGDKFAENDVI 229
Cdd:cd11709     1 GKWYWEVRVDSGNG-----------GLIQVGWATKSFSLDgeggVGDDEESWGYDGSRLRKgHGGSSGPGGRPWKSGDVV 69

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1007389400 230 GCFADFECGndvELSFTKNGKWMGIAFRIqkEALGGQALYPHV-LVKNCAVEFN 282
Cdd:cd11709    70 GCLLDLDEG---TLSFSLNGKDLGVAFTN--LFLKGGGLYPAVsLGSGQGVTIN 118
SPRY_RNF123 cd12882
SPRY domain at N-terminus of ring finger protein 123; This SPRY domain is found at the ...
 181-284 8.98e-16

SPRY domain at N-terminus of ring finger protein 123; This SPRY domain is found at the N-terminus of RING finger protein 123 domain (also known as E3 ubiquitin-protein ligase RNF123). The ring finger domain motif is present in a variety of functionally distinct proteins and known to be involved in protein-protein and protein-DNA interactions. RNF123 displays E3 ubiquitin ligase activity toward the cyclin-dependent kinase inhibitor p27 (Kip1).


Pssm-ID: 293940  Cd Length: 128  Bit Score: 74.29  E-value: 8.98e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007389400 181 VVRIGWSLDSC----STQLGEEPFSYGYGGTGKKSTNSRFENYGDKFAENDVIGCFADFECGndvELSFTKNGKWMGIAF 256
Cdd:cd12882    24 IMQIGWATISCrftqEEGVGDTRDSYAYDGNRVRKWNVSTQKYGEPWVAGDVIGCCIDLDKG---TISFYRNGRSLGVAF 100

                          90       100
                  ....*....|....*....|....*....
gi 1007389400 257 RiQKEALGGQALYPHV-LVKNCAVEFNFG 284
Cdd:cd12882   101 D-NVRRGPGLAYFPAVsLSFGERLELNFG 128
SPRY_RanBP_like cd12885
SPRY domain in Ran binding proteins, SSH4, HECT E3 and SPRYD3; This family includes SPRY ...
 159-284 2.77e-15

SPRY domain in Ran binding proteins, SSH4, HECT E3 and SPRYD3; This family includes SPRY domains found in Ran binding proteins (RBP or RanBPM) 9 and 10, SSH4 (suppressor of SHR3 null mutation protein 4), SPRY domain-containing protein 3 (SPRYD3) as well as HECT, a C-terminal catalytic domain of a subclass of ubiquitin-protein ligase (E3). RanBP9 and RanBP10 act as androgen receptor (AR) coactivators. Both consist of the N-terminal proline- and glutamine-rich regions, the SPRY domain, and LisH-CTLH and CRA motifs. The SPRY domain in SSH4 may be involved in cargo recognition, either directly or by combination with other adaptors, possibly leading to a higher selectivity. SPRYD3 is highly expressed in most tissues in humans, possibly involved in important cellular processes. HECT E3 mediates the direct transfer of ubiquitin from E2 to substrate.


Pssm-ID: 293943  Cd Length: 132  Bit Score: 73.08  E-value: 2.77e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007389400 159 FEMKINEEisvkhlpstePDPHVVRIGWSLDSCST--QLGEEPFSYGY-GGTGKKSTNS-RFENYGDKFAENDVIGCFAD 234
Cdd:cd12885    18 FEVTILDL----------GEKGIVSIGFCTSGFPLnrMPGWEDGSYGYhGDDGRVYLGGgEGENYGPPFGTGDVVGCGIN 87

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1007389400 235 FECGndvELSFTKNGKWMGIAFriqkEALGGQALYP--HVLVKNCAVEFNFG 284
Cdd:cd12885    88 FKTG---EVFFTKNGELLGTAF----ENVVKGRLYPtvGLGSPGVKVRVNFG 132
SPRY_RanBP9_10 cd12909
SPRY domain in Ran binding proteins 9 and 10; This family includes SPRY domain in Ran binding ...
 196-285 7.17e-10

SPRY domain in Ran binding proteins 9 and 10; This family includes SPRY domain in Ran binding protein (RBP or RanBPM) 9 and 10, and similar proteins. RanBP9 (also known as RanBPM), a binding partner of Ran, is a small Ras-like GTPase that exerts multiple functions via interactions with various proteins. RanBP9 and RanBP10 also act as androgen receptor (AR) coactivators. Both consist of the N-terminal proline- and glutamine-rich regions, the SPRY domain, and LisH-CTLH and CRA motifs. SPRY domain of RanBPM forms a complex with CD39, a prototypic member of the NTPDase family, thus down-regulating activity substantially. RanBP10 enhances the transcriptional activity of AR in a ligand-dependent manner and exhibits a protein expression pattern different from RanBPM in various cell lines. RanBP10 is highly expressed in AR-positive prostate cancer LNCaP cells, while RanBPM is abundant in WI-38 and MCF-7 cells.


Pssm-ID: 293966  Cd Length: 144  Bit Score: 57.92  E-value: 7.17e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007389400 196 GEEPFSYGY----------GGTGKKstnsrfenYGDKFAENDVIGCFADFEcgnDVELSFTKNGKWMGIAFRiqkeALGG 265
Cdd:cd12909    58 GWEPHSWGYhgddghsfcsSGTGKP--------YGPTFTTGDVIGCGINFR---DNTAFYTKNGVNLGIAFR----DIKK 122

                          90       100
                  ....*....|....*....|..
gi 1007389400 266 QALYPHVLVK--NCAVEFNFGQ 285
Cdd:cd12909   123 GNLYPTVGLRtpGEHVEANFGQ 144
COG4639 COG4639
Predicted kinase [General function prediction only];
320-478 9.46e-08

Predicted kinase [General function prediction only];


Pssm-ID: 443677 [Multi-domain]  Cd Length: 145  Bit Score: 51.75  E-value: 9.46e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007389400 320 ECEILMMVGLPAAGKTTWAIKHAASNPskkynILGTnaimDKMRVM-GLRR--QRNYAGRWDVLIQQATQCLnrliqiaa 396
Cdd:COG4639     1 MLSLVVLIGLPGSGKSTFARRLFAPTE-----VVSS----DDIRALlGGDEndQSAWGDVFQLAHEIARARL-------- 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007389400 397 RKKRNYILDQTNVygsaQRRKMRPFEGFQRK------AIVICPTDEDLKDRTIKRTdeegKDVPDHAVLEMKANF-TLPD 469
Cdd:COG4639    64 RAGRLTVVDATNL----QREARRRLLALARAygalvvAVVLDVPLEVCLARNAARD----RQVPEEVIRRMLRRLrRPPL 135


                  ....*....
gi 1007389400 470 VGDFLDEVL 478
Cdd:COG4639   136 PEEGFRVVY 144
SPRY2_RyR cd12878
SPRY domain 2 (SPRY2) of ryanodine receptor (RyR); This SPRY domain (SPRY2) is the second of ...
 146-252 1.17e-07

SPRY domain 2 (SPRY2) of ryanodine receptor (RyR); This SPRY domain (SPRY2) is the second of three structural repeats in all three isoforms of the ryanodine receptor (RyR), which are the major Ca2+ release channels in the membranes of sarcoplasmic reticulum (SR). There are three RyR genes in mammals; the skeletal RyR1, the cardiac RyR2 and the brain RyR3. The three SPRY domains are located in the N-terminal part of the cytoplasmic region of the RyRs, The SPRY2 domain has been shown to bind to the dihydropryidine receptor (DHPR) II-III loop and the ASI region of RyR1


Pssm-ID: 240458  Cd Length: 133  Bit Score: 51.15  E-value: 1.17e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007389400 146 ARASYGVRRGRVCFEMKINeeisvkhlpstepDPHVVRIGWSLDSC--STQLGEEPFSYGYGGTGKKSTNSRFENYGDKF 223
Cdd:cd12878     5 AEKTYAVTSGKWYFEFEVL-------------TSGYMRVGWARPGFrpDLELGSDDLSYAFDGFLARKWHQGSESFGKQW 71

                          90       100
                  ....*....|....*....|....*....
gi 1007389400 224 AENDVIGCFADFecgNDVELSFTKNGKWM 252
Cdd:cd12878    72 QPGDVVGCMLDL---VDRTISFTLNGELL 97
SPRY_SSH4_like cd12910
SPRY domain in SSH4 and similar proteins; This family includes SPRY domain in SSH4 (suppressor ...
 200-285 1.36e-04

SPRY domain in SSH4 and similar proteins; This family includes SPRY domain in SSH4 (suppressor of SHR3 null mutation protein 4) and similar proteins. SSH4 is a component of the endosome-vacuole trafficking pathway that regulates nutrient transport and may be involved in processes determining whether plasma membrane proteins are degraded or routed to the plasma membrane. The SPRY domain in SSH4 may be involved in cargo recognition, either directly or by combination with other adaptors, possibly leading to a higher selectivity. In yeast, SSH4 and the homologous protein EAR1 (endosomal adapter of RSP5) recruit Rsp5p, an essential ubiquitin ligase of the Nedd4 family, and assist it in its function at multivesicular bodies by directing the ubiquitylation of specific cargoes.


Pssm-ID: 293967  Cd Length: 192  Bit Score: 43.50  E-value: 1.36e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007389400 200 FSYGY-GGTGKKSTNSRF--ENYGDKFAENDVIGCFADFECGndvELSFTKNGK----WM-GIAFRIQKEAL----GGQA 267
Cdd:cd12910    94 GSLAVhSDDGHRYINDPFggKDFTPPFREGDTIGIGYRFSSG---TIFFTRNGKrlggWDlGEELDAEDDGVtgleGFHD 170

                          90       100
                  ....*....|....*....|
gi 1007389400 268 LYPHVLVKN--CAVEFNFGQ 285
Cdd:cd12910   171 LYAAIGVFGgeCEVHVNPGQ 190
SPRY_SOCS_Fbox cd12875
SPRY domain in Fbxo45 and suppressors of cytokine signaling (SOCS) proteins; This family ...
 145-272 9.97e-04

SPRY domain in Fbxo45 and suppressors of cytokine signaling (SOCS) proteins; This family consists of the SPRY domain-containing SOCS box protein family (SPSB1-4, also known as SSB-1 to -4) as well as F-box protein 45 (Fbxo45), a novel synaptic E3 and ubiquitin ligase. The SPSB protein is composed of a central SPRY protein interaction domain and a C-terminal SOCS box. SPSB1, SPSB2, and SPSB4 interact with prostate apoptosis response protein 4 (Par-4) and are negative regulators that recruit the ECS E3 ubiquitin ligase complex to polyubiquitinate inducible nitric-oxide synthase (iNOS), resulting in its proteasomal degradation. Fbxo45 is related to this family; it is located N-terminal to the SPRY domain, and known to induce the degradation of a synaptic vesicle-priming factor, Munc13-1, via the SPRY domain, thus playing an important role in the regulation of neurotransmission by modulating Munc13-1 at the synapse. Suppressor of cytokine signaling (SOCS) proteins negatively regulate signaling from JAK-associated cytokine receptor complexes, and play key roles in the regulation of immune homeostasis.


Pssm-ID: 293935  Cd Length: 169  Bit Score: 40.52  E-value: 9.97e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007389400 145 GARASYGVRRGRVCFEMKineeisvkhLPSTEPDPH-VVRIG-----WSLDSCSTQLGEEPFSYGYG-GTGK-----KST 212
Cdd:cd12875    32 AIRGKKGYTRGLHAWEVK---------WISRPRGSHaVVGVAtkdapLQCDGYVTLLGSNSESWGWDlGDNKlyhngKKV 102

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007389400 213 NSRFENYGDKFAENDVIGCFADFECGNdveLSFTKNGKWMGIAFRiqkeALGGQALYPHV 272
Cdd:cd12875   103 IGSYPAKSENYQVPDRILVILDMEDGT---LAFEANGEYLGVAFR----GLPGKLLYPAV 155
pseT PHA02530
polynucleotide kinase; Provisional
 320-352 5.32e-03

polynucleotide kinase; Provisional


Pssm-ID: 222856 [Multi-domain]  Cd Length: 300  Bit Score: 39.62  E-value: 5.32e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1007389400 320 ECEILMMVGLPAAGKTTWAIKHAASNPsKKYNI 352
Cdd:PHA02530    1 MMKIILTVGVPGSGKSTWAREFAAKNP-KAVNV 32
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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